Member database | SFLD |
SFLD type | family |
Short name | AMPS_(cytGST):_Alpha-__Mu-__Pi |
Description
The AMPS: Alpha-, Mu-, Pi-, and Sigma-like subgroup of cytosolic GSTs (cytGSTs) is associated primarily with eukaryotes. Members of this subgroup are associated with a number of human cancers and other diseases. GSTs in this subgroup use a tyrosine that is extended from the first beta sheet of the Trx fold to lower the pKa of glutathione; this does not correspond to either position of the classic thioredoxin CxxC motif. These cytGSTs include the proteins from the alpha, mu, pi, and sigma classes. Proteins in this subgroup are known to catalyze the following reaction types: conjugate addition, epoxide ring opening, isomerization, nucleophilic addition, nucleophilic aromatic substitution, nucleophilic substitution (SN2), and peroxidase reactions. For example, SFLD protein 55701 (UniProt accn O60760) has experimentally-confirmed nucleophilic aromatic substitution activity with CDNB and peroxidase activity, specifically prostaglandin-D synthase activity, with prostaglandin H2
[2, 1].
References
1.Mammalian cytosolic glutathione transferases. Dourado DF, Fernandes PA, Ramos MJ. Curr Protein Pept Sci 9, 325-37, (2008). PMID: 18691123
2.Structure, catalytic mechanism, and evolution of the glutathione transferases. Armstrong RN. Chem. Res. Toxicol. 10, 2-18, (1997). View articlePMID: 9074797
External Links
Representative structure
2vcz: Complex structure of prostaglandin D2 synthase at 1.95A.